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Database: UniProt
Entry: A0A3P9C2E0_9CICH
LinkDB: A0A3P9C2E0_9CICH
Original site: A0A3P9C2E0_9CICH 
ID   A0A3P9C2E0_9CICH        Unreviewed;      1143 AA.
AC   A0A3P9C2E0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Integrin alpha-L {ECO:0000313|Ensembl:ENSMZEP00005016277.1};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005016277.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005016277.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005016277.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR   AlphaFoldDB; A0A3P9C2E0; -.
DR   STRING; 106582.ENSMZEP00005016277; -.
DR   Ensembl; ENSMZET00005016796.1; ENSMZEP00005016277.1; ENSMZEG00005012209.1.
DR   GeneTree; ENSGT00940000154838; -.
DR   Proteomes; UP000265160; LG6.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR048633; ITGAX-like_Ig_3.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF134; INTEGRIN ALPHA-L ISOFORM X1; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF21520; ITGAX-like_Ig_3; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 2.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS51470; FG_GAP; 4.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003762};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   TRANSMEM        1075..1097
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   DOMAIN          150..325
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REPEAT          378..430
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          431..493
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          494..550
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          555..617
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ   SEQUENCE   1143 AA;  128091 MW;  BB5C82927014FC51 CRC64;
     MLFTFSASTI PACLAFNIDT RNPEVFLGEP GDFFGYRVLQ YLNKSSNNKG IVVTAPLRLN
     GSGGIYQPHQ NKWFKPTEDL QSNTTAVKHL GLSIAADSSG SRFTVCSPSL VHECNENSYL
     NSICYELSDQ LQKISSFKPA YQECTKKTVD LVFLFDGSAS MTEEEFNRNN DFIVEIMDSL
     KNMSIKFAAV QFSSTVHKVF DFNDYKAGRA LDKLMKENHL KGLTNTHRAI EFVLDQIFDN
     PAAGASPDAT KALILITDGD PSDTDRKGII KKYDEKNIIR LVIGIKDAKL DKFRAIASEP
     KDKNAFKIEN YDGLTGVLEN FQKDVFVMEG SKGAQARNLT DEMSQSGFSA IFNKDTLILG
     SVGTNSWRGS LQERRDKTET IEDQEMEMDS YMGYSVSVGE RGGVSLYFTG APRFQHTGQV
     VLFKQNSNNW TTAQRITGDQ IGSYFGAELC SVDINSDGDT DFLLVGAPTF YQLQEKKEGQ
     IYIYTLTDEL QLKSELIVMG PSMGRFGTTI SSLADLNGDE LRDVAVGAPL EDDNRGAVYI
     YHGNKQRGIC STFSQRITGK EVTPGIKFFG QAIDGAIDLG GNGLPDIVIG SQGAAVVFRY
     QNSPIFDVMA HLTFQPKEIN TEIFDCLGAD ENLPMVTLTA CFEMVKVTKS KQEAVRSGLN
     ITFTVAVDPM RQKYRGFFSQ TDKTARSLTS TYEMLDETAC FNFSIYMHKC VSELLSPISI
     KCNFSQADNE TAATTLNVDS KRQSVVEVPF KKACRKNDTC IAELDVDFSF MTTQLLVAED
     AYFNVSIKLA NHGDDSYNTM LAMHYPPGLS FSRMTLIESS RSTPHKCSDL EGVLDKTICG
     VSLPLFRSRS SATFESSFYV MHDFEWDDTI SMTIDANSNN QDSNRTSALT KNIPVQYEIK
     MILTVKQDSA TYLNFTTEDP APKEMGITYR IDNFGFKDFP VNVTMFFPTE LEHNFEIKSY
     EVFVKEVTLC LPEHFSCITM VCKSFNLEKY SAAEFTLLGK ANFRDLEQKP ANLPFLKKYT
     GDSGNVKFVS SIHVGYNKDR FVLESLKQKV FFTHSNNTTR WIEVQFDFII PPNKLLIIST
     GVSLGLVLLI VITVVLFKLG CFKRRKLTYH IQRERIKATE NVEETKVQIF LIYNYSEGVN
     LNI
//
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